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Dimeric molecular motors walk on polar tracks by binding and hydrolyzing oneATP per step. Despite tremendous progress, the waiting state for ATP binding inthe well-studied kinesin that walks on microtubule (MT), remains controversial.One experiment suggests that in the waiting state both heads are bound to theMT, while the other shows that ATP binds to the leading head after the partnerhead detaches. To discriminate between these two scenarios, we developed atheory to calculate accurately several experimentally measurable quantities asa function of ATP concentration and resistive force.  In particular, we predict that measurement of the randomness parameter coulddiscriminate between the two scenarios for the waiting state of kinesin,thereby resolving this standing controversy.

How kinesin waits for ATP affects the nucleotide and load dependence of the stepping kinetics